2WUL
CRYSTAL STRUCTURE OF THE HUMAN GLUTAREDOXIN 5 WITH BOUND GLUTATHIONE IN AN FES CLUSTER
Replaces: 2WEMExperimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SLS BEAMLINE X10SA |
| Synchrotron site | SLS |
| Beamline | X10SA |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2007-12-08 |
| Detector | MARRESEARCH |
| Wavelength(s) | 0.979, 0.9794 |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 68.995, 68.995, 229.331 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 66.070 - 2.400 |
| R-factor | 0.20216 |
| Rwork | 0.200 |
| R-free | 0.25079 |
| Structure solution method | SAD |
| Starting model (for MR) | 2e7p |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.306 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | SHELX |
| Refinement software | REFMAC (5.5.0102) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 69.050 | 2.530 |
| High resolution limit [Å] | 2.400 | 2.400 |
| Rmerge | 0.190 | 0.960 |
| Number of reflections | 22752 | |
| <I/σ(I)> | 9.2 | 2 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 6.9 | 6.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 6.5 | 50% PEG300, 0.2 M MGCL2, 0.1 M CACODYLATE PH 6.5, 0.01 M SPERMINE TETRAHYDROCHLORIDE |
